The lipase of Thermomyces lanuginosus (also known as Humicola lanuginosa) is known to be useful for various industrial purposes such as detergents and baking (EP 258068, WO 9404035). Its amino acid and DNA sequences are shown in U.S. Pat. No. 5,869,438.
The prior art describes the modification of the amino acid sequence of the T. lanuginosus lipase to create variants with the aim of modifying the enzyme properties. Thus, U.S. Pat. No. 5,869,438, WO 95/22615, WO 97/04079 and WO 00/32758 disclose the use of mutagenesis of the lipase gene to produce such variants. WO 00/32758 also discloses the construction of variants with the backbone from T. lanuginosus lipase and C-terminal from Fusarium oxysporum phospholipase by PCR reaction.
Crameri et al., Nature, 391: 288-291 (1998) discloses DNA shuffling of a family of naturally occurring homologous genes from diverse species to create diversity into proteins. U.S. Pat. No. 6,159,687 discloses shuffling of genes encoding variants of the T. lanuginosus lipase. WO 98/41623 discloses shuffling of heterologous polynucleotide sequences.
The following published sequences of lipolytic enzymes from Aspergillus have amino acid identities of 49-51% to the T. lanuginosus lipase: Lysophospholipase from A. foetidus (EMBL A93428, U.S. Pat. No. 6,140,094), lipase from A. tubingensis (EMBL A84589, WO 9845453), phospholipase A1 from A. oryzae (EMBL E16314, EP 575133, JP 10155493 A) and Lysophospholipase from A. niger (EMBL A90761, WO 98/31790).
R. Lattmann et al., Biocatalysis, 3 (1-2): 137-144 (1990) disclose an esterase from Talaromyces thermophilus. V. W. Ogundero, Mycologia, 72 (1): 118-126 (1980) describes the lipase activity of Talaromyces thermophilus. U.S. Pat. No. 4,275,011 and EP 258068 refer to a lipase from Thermomyces ibadanensis. B. A. Oso, Canadian Journal of Botany, 56: 1840-1843 (1978) describes the lipase activity of Talaromyces emersonii. 